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Advantages of using CPMV particles as a vaccine delivery system include the natural resistance of CPMV to high temperature, low pH and proteolysis as well as the potential for large-scale production in the natural host black-eyed pea or Vigna unguiculata (≥1.0 g of virus per kilogram of leaves).
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To that end, in this work we have studied the relationship between the surface antigen (the glycoptoyein G) of 3 viruses belonging to the Rhabdoviridae family (VSV, VHSV, and SVCV) and autophagy.
We generated particles pseudotyped with HCV envelope glycoproteins from 1a and 2a genotypes (HCVpp 1a and HCVpp 2a, respectively) and control particles pseudotyped with the envelope glycoprotein G of vesicular stomatitis virus (VSVpp).
In addition, the glycoprotein G (G) of 3 different viruses, a mammalian rhabdovirus (VSV), and 2 fish rhabdoviruses (viral hemorrhagic septicemia virus, VHSV, and spring viremia of carp virus, SVCV) were used to study both in vitro and in vivo their potential to induce autophagy in the model vertebrate species zebrafish (Danio rerio).
Such a %G + C bias in Nextera library preps is not entirely surprising as previous work demonstrated reduced coverage in both high and low %G + C regions of virus genomes [ 34], presumably due to non-random transposition.
Respective vaccine efficacy was also calculated for each G- and P- type of virus with 95% CI.
Note that c, g, and δ include the removal of virus, and of the uninfected and infected cells, due to the experimental samplings.
Then, a highly concentrated viral stock of 0.5 1.5 ml was added per well and centrifuged for 2 h at 1500 g at 32 °C to facilitate attachment of virus particles onto RetroNectin.
This vector, combining the signal peptide of the single major envelope glycoprotein gp64 from AcMNPV with the cytoplasmic and transmembrane domains of VSV-G vesicular stomatitis virus G glycoprotein, allows a high level of displayed proteins as well as alternate presentation of epitopes independent of gp64 [ 12].
The RNA genome of hepatitis G virus (HGV) encodes a large polyprotein that is processed to mature proteins by viral-encoded proteases.
Whereas the F gene was relatively conserved between subgroups, a high degree of variation was observed in the extracellular domain of the G gene of the virus.
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